Structural highlights
Function
FPN_BDEBA Iron transpoter that exports Fe(2+) from the cell. Also binds to Co(2+) and Ni(2+). May act as a multivalent divalent metal transporter (PubMed:26608034). The transporter is composed of 12 transmembrane (TM) helices organized into N-terminal (TM1-6) and C-terminal (TM7-12) domains. The substrate-binding site is formed at the interface of the two domains and is alternately accessible from either side of the membrane. The transport cycle is viewed as a series of ligand-induced conformational changes that include open outward and open inward states (PubMed:26461048, PubMed:30082682).[1] [2] [3]
References
- ↑ Taniguchi R, Kato HE, Font J, Deshpande CN, Wada M, Ito K, Ishitani R, Jormakka M, Nureki O. Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin. Nat Commun. 2015 Oct 13;6:8545. doi: 10.1038/ncomms9545. PMID:26461048 doi:https://dx.doi.org/10.1038/ncomms9545
- ↑ Bonaccorsi di Patti MC, Polticelli F, Tortosa V, Furbetta PA, Musci G. A bacterial homologue of the human iron exporter ferroportin. FEBS Lett. 2015 Dec 21;589(24 Pt B):3829-35. PMID:26608034 doi:10.1016/j.febslet.2015.11.025
- ↑ Deshpande CN, Ruwe TA, Shawki A, Xin V, Vieth KR, Valore EV, Qiao B, Ganz T, Nemeth E, Mackenzie B, Jormakka M. Calcium is an essential cofactor for metal efflux by the ferroportin transporter family. Nat Commun. 2018 Aug 6;9(1):3075. doi: 10.1038/s41467-018-05446-4. PMID:30082682 doi:https://dx.doi.org/10.1038/s41467-018-05446-4
